dbPTM

DPYL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DPYL2_HUMAN
UniProt AC	Q16555
Protein Name	Dihydropyrimidinase-related protein 2
Gene Name	DPYSL2
Organism	Homo sapiens (Human).
Sequence Length	572
Subcellular Localization	Cytoplasm, cytosol . Cytoplasm, cytoskeleton . Membrane . Tightly but non-covalently associated with membranes.
Protein Description	Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis..
Protein Sequence	MSYQGKKNIPRITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLAELRGVPRGLYDGPVCEVSVTPKTVTPASSAKTSPAKQQAPPVRNLHQSGFSLSGAQIDDNIPRRTTQRIVAPPGGRANITSLG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSYQGKKNI ------CCCCCCCCC	26.60	21406692
3	Phosphorylation	-----MSYQGKKNIP -----CCCCCCCCCC	21.71	18083107
7	Phosphorylation	-MSYQGKKNIPRITS -CCCCCCCCCCCCCC	67.92	24719451
13	Phosphorylation	KKNIPRITSDRLLIK CCCCCCCCCCCEEEE	26.34	28450419
14	Phosphorylation	KNIPRITSDRLLIKG CCCCCCCCCCEEEEC	20.54	28450419
20	Acetylation	TSDRLLIKGGKIVND CCCCEEEECCEECCC	62.67	25953088
25	Phosphorylation	LIKGGKIVNDDQSFY EEECCEECCCCCCCH	7.97	24719451
27	Phosphorylation	KGGKIVNDDQSFYAD ECCEECCCCCCCHHE	44.42	-
30	Phosphorylation	KIVNDDQSFYADIYM EECCCCCCCHHEEEE	27.50	24076635
32	Phosphorylation	VNDDQSFYADIYMED CCCCCCCHHEEEECC	14.49	24927040
43	Ubiquitination	YMEDGLIKQIGENLI EECCCCHHEECCCEE	40.69	-
54	Phosphorylation	ENLIVPGGVKTIEAH CCEEECCCCCEEEEC	16.21	-
56	Phosphorylation	LIVPGGVKTIEAHSR EEECCCCCEEEECCC	47.24	24719451
57	Phosphorylation	IVPGGVKTIEAHSRM EECCCCCEEEECCCE	22.95	-
59	Methylation	PGGVKTIEAHSRMVI CCCCCEEEECCCEEE	45.63	-
64	Sulfoxidation	TIEAHSRMVIPGGID EEEECCCEEECCCCC	3.43	30846556
74	Phosphorylation	PGGIDVHTRFQMPDQ CCCCCEEECCCCCCC	32.78	-
78	Sulfoxidation	DVHTRFQMPDQGMTS CEEECCCCCCCCCCC	3.48	21406390
82	Phosphorylation	RFQMPDQGMTSADDF CCCCCCCCCCCHHHH	28.81	-
83	Phosphorylation	FQMPDQGMTSADDFF CCCCCCCCCCHHHHH	1.91	-
83	Sulfoxidation	FQMPDQGMTSADDFF CCCCCCCCCCHHHHH	1.91	30846556
85	Phosphorylation	MPDQGMTSADDFFQG CCCCCCCCHHHHHHH	22.32	-
94	Phosphorylation	DDFFQGTKAALAGGT HHHHHHHHHHHCCCC	38.19	-
97	Phosphorylation	FQGTKAALAGGTTMI HHHHHHHHCCCCEEE	5.63	-
101	Phosphorylation	KAALAGGTTMIIDHV HHHHCCCCEEEEEEE	16.57	-
102	Phosphorylation	AALAGGTTMIIDHVV HHHCCCCEEEEEEEC	15.06	22798277
103	Sulfoxidation	ALAGGTTMIIDHVVP HHCCCCEEEEEEECC	2.25	30846556
107	Phosphorylation	GTTMIIDHVVPEPGT CCEEEEEEECCCCCC	16.44	24719451
152	Sulfoxidation	HKGIQEEMEALVKDH HHHHHHHHHHHHHHH	3.43	21406390
168	Sulfoxidation	VNSFLVYMAFKDRFQ CCCHHHHHHCCCCCC	2.49	30846556
241	O-linked_Glycosylation	EAVNRAITIANQTNC HHHHHHHHHHHHCCC	17.04	28510447
246	Phosphorylation	AITIANQTNCPLYIT HHHHHHHCCCCEEEE	38.30	24076635
251	Phosphorylation	NQTNCPLYITKVMSK HHCCCCEEEEEECCC	7.53	28152594
253	Phosphorylation	TNCPLYITKVMSKSS CCCCEEEEEECCCCH	12.20	28152594
254	Acetylation	NCPLYITKVMSKSSA CCCEEEEEECCCCHH	26.78	25953088
254	Ubiquitination	NCPLYITKVMSKSSA CCCEEEEEECCCCHH	26.78	-
258	Succinylation	YITKVMSKSSAEVIA EEEEECCCCHHHHHH	30.27	-
258	Succinylation	YITKVMSKSSAEVIA EEEEECCCCHHHHHH	30.27	-
258	Ubiquitination	YITKVMSKSSAEVIA EEEEECCCCHHHHHH	30.27	-
259	Phosphorylation	ITKVMSKSSAEVIAQ EEEECCCCHHHHHHH	27.72	-
269	Ubiquitination	EVIAQARKKGTVVYG HHHHHHHHCCEEEEC	59.58	-
270	Ubiquitination	VIAQARKKGTVVYGE HHHHHHHCCEEEECC	55.02	-
280	Phosphorylation	VVYGEPITASLGTDG EEECCCEEEEECCCC	22.40	-
282	Phosphorylation	YGEPITASLGTDGSH ECCCEEEEECCCCCC	20.77	28348404
285	Phosphorylation	PITASLGTDGSHYWS CEEEEECCCCCCCCC	42.34	28348404
288	Phosphorylation	ASLGTDGSHYWSKNW EEECCCCCCCCCCCH	19.06	25159151
290	Phosphorylation	LGTDGSHYWSKNWAK ECCCCCCCCCCCHHH	17.05	27251275
292	Phosphorylation	TDGSHYWSKNWAKAA CCCCCCCCCCHHHHE	14.67	24076635
293	Acetylation	DGSHYWSKNWAKAAA CCCCCCCCCHHHHEE	42.22	25953088
293	Ubiquitination	DGSHYWSKNWAKAAA CCCCCCCCCHHHHEE	42.22	-
303	Phosphorylation	AKAAAFVTSPPLSPD HHHEEEECCCCCCCC	29.12	20068231
304	Phosphorylation	KAAAFVTSPPLSPDP HHEEEECCCCCCCCC	21.15	20068231
308	Phosphorylation	FVTSPPLSPDPTTPD EECCCCCCCCCCCHH	32.79	21406692
345	Acetylation	TAQKAVGKDNFTLIP CHHHHHCCCCEEEEC	42.79	66723665
345	Ubiquitination	TAQKAVGKDNFTLIP CHHHHHCCCCEEEEC	42.79	-
358	Phosphorylation	IPEGTNGTEERMSVI ECCCCCCCCHHEEEE	36.42	-
363	Phosphorylation	NGTEERMSVIWDKAV CCCCHHEEEEEEEEE	19.37	25332170
368	2-Hydroxyisobutyrylation	RMSVIWDKAVVTGKM HEEEEEEEEEEECCC	28.25	-
368	Ubiquitination	RMSVIWDKAVVTGKM HEEEEEEEEEEECCC	28.25	-
374	Ubiquitination	DKAVVTGKMDENQFV EEEEEECCCCCCCEE	33.54	-
390	Ubiquitination	VTSTNAAKVFNLYPR EEECCHHHHCCCCCC	44.97	-
393	Phosphorylation	TNAAKVFNLYPRKGR CCHHHHCCCCCCCCC	41.47	27251275
416	Phosphorylation	LVIWDPDSVKTISAK EEEECCCCCEEEEEE	30.79	-
418	Ubiquitination	IWDPDSVKTISAKTH EECCCCCEEEEEECC	44.06	-
423	Acetylation	SVKTISAKTHNSSLE CCEEEEEECCCCCCC	43.45	25953088
423	Ubiquitination	SVKTISAKTHNSSLE CCEEEEEECCCCCCC	43.45	-
424	Phosphorylation	VKTISAKTHNSSLEY CEEEEEECCCCCCCE	26.46	30108239
427	Phosphorylation	ISAKTHNSSLEYNIF EEEECCCCCCCEEEE	28.79	30108239
428	Phosphorylation	SAKTHNSSLEYNIFE EEECCCCCCCEEEEC	30.45	28464451
431	Phosphorylation	THNSSLEYNIFEGME CCCCCCCEEEECCCC	20.89	30108239
437	Sulfoxidation	EYNIFEGMECRGSPL CEEEECCCCCCCCCE	3.28	30846556
442	Phosphorylation	EGMECRGSPLVVISQ CCCCCCCCCEEEEEC	8.84	30266825
448	Phosphorylation	GSPLVVISQGKIVLE CCCEEEEECCEEEEC	22.67	30266825
458	Phosphorylation	KIVLEDGTLHVTEGS EEEECCCCEEEEECC	26.47	24076635
462	Phosphorylation	EDGTLHVTEGSGRYI CCCCEEEEECCCCCC	24.71	19060867
465	Phosphorylation	TLHVTEGSGRYIPRK CEEEEECCCCCCCCC	17.54	28857561
472	Ubiquitination	SGRYIPRKPFPDFVY CCCCCCCCCCCCHHH	45.73	21890473
472	Ubiquitination	SGRYIPRKPFPDFVY CCCCCCCCCCCCHHH	45.73	21890473
472	Malonylation	SGRYIPRKPFPDFVY CCCCCCCCCCCCHHH	45.73	26320211
472	Ubiquitination	SGRYIPRKPFPDFVY CCCCCCCCCCCCHHH	45.73	21890473
479	Phosphorylation	KPFPDFVYKRIKARS CCCCCHHHHHHHHHH	8.44	19276087
480	2-Hydroxyisobutyrylation	PFPDFVYKRIKARSR CCCCHHHHHHHHHHH	42.20	-
492	Methylation	RSRLAELRGVPRGLY HHHHHHHHCCCCCCC	35.25	-
499	Phosphorylation	RGVPRGLYDGPVCEV HCCCCCCCCCCEEEE	22.98	21945579
504	S-nitrosocysteine	GLYDGPVCEVSVTPK CCCCCCEEEEEEECC	4.87	-
504	S-nitrosylation	GLYDGPVCEVSVTPK CCCCCCEEEEEEECC	4.87	19483679
504	S-palmitoylation	GLYDGPVCEVSVTPK CCCCCCEEEEEEECC	4.87	26865113
507	O-linked_Glycosylation	DGPVCEVSVTPKTVT CCCEEEEEEECCCCC	9.66	28510447
507	Phosphorylation	DGPVCEVSVTPKTVT CCCEEEEEEECCCCC	9.66	21945579
509	O-linked_Glycosylation	PVCEVSVTPKTVTPA CEEEEEEECCCCCCC	16.15	28510447
509	Phosphorylation	PVCEVSVTPKTVTPA CEEEEEEECCCCCCC	16.15	19664994
511	Ubiquitination	CEVSVTPKTVTPASS EEEEEECCCCCCCCC	46.38	-
512	O-linked_Glycosylation	EVSVTPKTVTPASSA EEEEECCCCCCCCCC	30.71	28510447
512	Phosphorylation	EVSVTPKTVTPASSA EEEEECCCCCCCCCC	30.71	26846344
514	Phosphorylation	SVTPKTVTPASSAKT EEECCCCCCCCCCCC	20.54	15466863
517	O-linked_Glycosylation	PKTVTPASSAKTSPA CCCCCCCCCCCCCCH	31.84	28510447
517	Phosphorylation	PKTVTPASSAKTSPA CCCCCCCCCCCCCCH	31.84	26846344
518	Phosphorylation	KTVTPASSAKTSPAK CCCCCCCCCCCCCHH	35.57	15466863
520	2-Hydroxyisobutyrylation	VTPASSAKTSPAKQQ CCCCCCCCCCCHHHC	52.03	-
520	Acetylation	VTPASSAKTSPAKQQ CCCCCCCCCCCHHHC	52.03	25953088
520	Ubiquitination	VTPASSAKTSPAKQQ CCCCCCCCCCCHHHC	52.03	-
521	Phosphorylation	TPASSAKTSPAKQQA CCCCCCCCCCHHHCC	39.39	26846344
522	Phosphorylation	PASSAKTSPAKQQAP CCCCCCCCCHHHCCC	23.35	15466863
525	Acetylation	SAKTSPAKQQAPPVR CCCCCCHHHCCCCCC	46.45	7340157
525	Ubiquitination	SAKTSPAKQQAPPVR CCCCCCHHHCCCCCC	46.45	-
533	Phosphorylation	QQAPPVRNLHQSGFS HCCCCCCCCCCCCCC	41.95	24719451
537	O-linked_Glycosylation	PVRNLHQSGFSLSGA CCCCCCCCCCCCCCC	30.93	28510447
537	Phosphorylation	PVRNLHQSGFSLSGA CCCCCCCCCCCCCCC	30.93	30266825
540	Phosphorylation	NLHQSGFSLSGAQID CCCCCCCCCCCCCCC	25.75	23401153
542	Phosphorylation	HQSGFSLSGAQIDDN CCCCCCCCCCCCCCC	30.77	30266825
554	Phosphorylation	DDNIPRRTTQRIVAP CCCCCCCCCCEEECC	28.67	22210691
555	Phosphorylation	DNIPRRTTQRIVAPP CCCCCCCCCEEECCC	17.65	10818093
565	Asymmetric dimethylarginine	IVAPPGGRANITSLG EECCCCCCCCCCCCC	30.31	-
565	Methylation	IVAPPGGRANITSLG EECCCCCCCCCCCCC	30.31	-
569	Phosphorylation	PGGRANITSLG---- CCCCCCCCCCC----	20.08	23403867
570	O-linked_Glycosylation	GGRANITSLG----- CCCCCCCCCC-----	27.57	28510447
570	Phosphorylation	GGRANITSLG----- CCCCCCCCCC-----	27.57	29514088
614	Phosphorylation	------------------------------------------------- -------------------------------------------------		24719451
619	Phosphorylation	------------------------------------------------------ ------------------------------------------------------		24719451
623	Phosphorylation	---------------------------------------------------------- ----------------------------------------------------------		24719451
626	Phosphorylation	------------------------------------------------------------- -------------------------------------------------------------		27251275
627	Phosphorylation	-------------------------------------------------------------- --------------------------------------------------------------		24719451
642	Phosphorylation	----------------------------------------------------------------------------- -----------------------------------------------------------------------------		24719451
645	Phosphorylation	-------------------------------------------------------------------------------- --------------------------------------------------------------------------------		24719451
647	Phosphorylation	---------------------------------------------------------------------------------- ----------------------------------------------------------------------------------		24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
32	Y	Phosphorylation	Kinase	FYN	P06241	Uniprot
479	Y	Phosphorylation	Kinase	FER	P16591	PSP
479	Y	Phosphorylation	Kinase	YES1	P07947	GPS
499	Y	Phosphorylation	Kinase	FER	P16591	PSP
509	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
514	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
518	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
518	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
522	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
522	S	Phosphorylation	Kinase	DYRK2	Q92630	Uniprot
555	T	Phosphorylation	Kinase	ROCK1	Q13464	PSP
555	T	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
555	T	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
555	T	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
509	T	Phosphorylation	10757975
3F4, a monoclonal antibody which strongly stains neurofibrillary tangles in Alzheimer disease brains, specifically labels DPYSL2 when phosphorylated on Ser-518, Ser-522 and Thr-509.
514	T	Phosphorylation	10757975
Phosphorylation at Thr-514 by GSK3B abolishes tubulin-binding leading to destabilization of microtubule assembly in axons and neurodegeneration (By similarity).
518	S	Phosphorylation	10757975
3F4, a monoclonal antibody which strongly stains neurofibrillary tangles in Alzheimer disease brains, specifically labels DPYSL2 when phosphorylated on Ser-518, Ser-522 and Thr-509.
522	S	Phosphorylation	10757975
3F4, a monoclonal antibody which strongly stains neurofibrillary tangles in Alzheimer disease brains, specifically labels DPYSL2 when phosphorylated on Ser-518, Ser-522 and Thr-509.
522	S	Phosphorylation	10757975
Phosphorylation by DYRK2 at Ser-522 is required for subsequent phosphorylation by GSK3B.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DPYL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AP2A1_HUMAN	AP2A1	physical	12942088
NUMB_HUMAN	NUMB	physical	12942088
DPYL1_HUMAN	CRMP1	physical	21900206
DPYL4_HUMAN	DPYSL4	physical	21900206
TBB5_BOVIN	TUBB	physical	12134159
LEF1_HUMAN	LEF1	physical	21988832
HS105_HUMAN	HSPH1	physical	22863883
PDE3A_HUMAN	PDE3A	physical	22863883
PUS7_HUMAN	PUS7	physical	22863883
RNBP6_HUMAN	RANBP6	physical	22863883
DPYL2_HUMAN	DPYSL2	physical	25416956
DPYL3_HUMAN	DPYSL3	physical	25416956
GORS2_HUMAN	GORASP2	physical	25416956
DPYL5_HUMAN	DPYSL5	physical	25416956
ARFP1_HUMAN	ARFIP1	physical	26344197
NTM1A_HUMAN	NTMT1	physical	26344197
VPS28_HUMAN	VPS28	physical	26344197
DPYL2_HUMAN	DPYSL2	physical	21516116

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DPYL2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509; THR-512; THR-514;SER-518; THR-521 AND SER-522, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Neurofibrillary tangle-associated collapsin response mediatorprotein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518, andSer-522."; Gu Y., Hamajima N., Ihara Y.; Biochemistry 39:4267-4275(2000). Cited for: PHOSPHORYLATION AT SER-518; SER-522 AND THR-509, AND MUTAGENESIS OFSER-507; THR-509; THR-512; THR-514; SER-517; SER-518; THR-521 ANDSER-522.	10757975 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND MASSSPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-32, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Semaphorin3A signaling mediated by Fyn-dependent tyrosinephosphorylation of collapsin response mediator protein 2 at tyrosine32."; Uchida Y., Ohshima T., Yamashita N., Ogawara M., Sasaki Y.,Nakamura F., Goshima Y.; J. Biol. Chem. 284:27393-27401(2009). Cited for: PHOSPHORYLATION AT TYR-32 BY FYN.	19652227 [Abstract]

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